ID   DMP_BPT5                Reviewed;         244 AA.
AC   Q38167; Q66LQ4; Q6QGT6;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 2.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=5'-deoxynucleotidase;
DE            EC=3.1.3.89 {ECO:0000269|PubMed:21305};
DE   AltName: Full=Deoxynucleoside-5'-monophosphatase;
DE            Short=5'-dNMPase;
DE   AltName: Full=Protein dmp;
GN   Name=dmp;
GN   ORFNames=T5.001 {ECO:0000312|EMBL:AAS77048.1},
GN   T5p001 {ECO:0000312|EMBL:AAU05154.1};
GN   and
GN   Name=T5p159 {ECO:0000312|EMBL:AAU05298.1};
OS   Escherichia phage T5 (Enterobacteria phage T5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Demerecviridae; Markadamsvirinae; Tequintavirus.
OX   NCBI_TaxID=2695836;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ksenzenko V.N., Kaliman A.V., Krutilina A.I., Shlyapnikov M.G.;
RT   "Bacteriophage T5 complete genome.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11303-B5;
RX   PubMed=15661140; DOI=10.1016/j.virol.2004.10.049;
RA   Wang J., Jiang Y., Vincent M., Sun Y., Yu H., Wang J., Bao Q., Kong H.,
RA   Hu S.;
RT   "Complete genome sequence of bacteriophage T5.";
RL   Virology 332:45-65(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=St0 deletion mutant;
RX   PubMed=24198424; DOI=10.1128/jvi.02262-13;
RA   Zivanovic Y., Confalonieri F., Ponchon L., Lurz R., Chami M., Flayhan A.,
RA   Renouard M., Huet A., Decottignies P., Davidson A.R., Breyton C.,
RA   Boulanger P.;
RT   "Insights into bacteriophage T5 structure from analysis of its
RT   morphogenesis genes and protein components.";
RL   J. Virol. 88:1162-1174(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 161-244.
RX   PubMed=8057856; DOI=10.1111/j.1365-2958.1994.tb01020.x;
RA   Decker K., Krauel V., Meesmann A., Heller K.J.;
RT   "Lytic conversion of Escherichia coli by bacteriophage T5: blocking of the
RT   FhuA receptor protein by a lipoprotein expressed early during infection.";
RL   Mol. Microbiol. 12:321-332(1994).
RN   [5]
RP   CHARACTERIZATION, CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=21305; DOI=10.1128/jvi.24.2.635-641.1977;
RA   Mozer T.J., Warner H.R.;
RT   "Properties of deoxynucleoside 5'-monophosphatase induced by bacteriophage
RT   T5 after infection of Escherichia coli.";
RL   J. Virol. 24:635-641(1977).
RN   [6]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=335083; DOI=10.1128/jvi.24.2.642-650.1977;
RA   Mozer T.J., Thompson R.B., Berget S.M., Warner H.R.;
RT   "Isolation and characterization of a bacteriophage T5 mutant deficient in
RT   deoxynucleoside 5'-monophosphatase activity.";
RL   J. Virol. 24:642-650(1977).
CC   -!- FUNCTION: Following host DNA degradation, is responsible for the
CC       degradation of 5'-dNMP's to deoxynucleosides that can be further
CC       excreted (PubMed:335083). Active on deoxynucleoside 5'-monophosphates
CC       but not active as a phosphatase on ribonucleotides, deoxynucleoside 5'-
CC       triphosphates, deoxynucleoside 3'-monophosphates, or
CC       deoxyoligonucleotides (PubMed:21305). {ECO:0000269|PubMed:21305,
CC       ECO:0000269|PubMed:335083}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-
CC         deoxyribonucleoside + phosphate; Xref=Rhea:RHEA:36167,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:18274, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:65317; EC=3.1.3.89;
CC   -!- INDUCTION: Expressed pre-early in the viral replicative cycle.
CC       Expressed with a few other proteins from the first step transfer (FST)
CC       DNA. FST DNA corresponds to the first small portion of the genome that
CC       enters into the host cell at the beginning of infection before pausing.
CC       {ECO:0000303|PubMed:335083}.
CC   -!- MISCELLANEOUS: This gene is part of the long terminal repeats present
CC       at both ends of the viral genome and is thus duplicated.
CC       {ECO:0000269|PubMed:15661140}.
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DR   EMBL; AY543070; AAS77048.1; -; Genomic_DNA.
DR   EMBL; AY692264; AAU05154.1; -; Genomic_DNA.
DR   EMBL; AY692264; AAU05298.1; -; Genomic_DNA.
DR   EMBL; AY587007; AAX11938.1; -; Genomic_DNA.
DR   EMBL; AY587007; AAX12089.1; -; Genomic_DNA.
DR   EMBL; X75922; CAA53525.1; -; Genomic_DNA.
DR   PIR; S44989; S44989.
DR   RefSeq; YP_006829.1; NC_005859.1.
DR   GeneID; 2777573; -.
DR   KEGG; vg:2777573; -.
DR   Proteomes; UP000002107; Genome.
DR   Proteomes; UP000002141; Genome.
DR   Proteomes; UP000002503; Genome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0039637; P:catabolism by virus of host DNA; IDA:UniProtKB.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023214; HAD_sf.
PE   1: Evidence at protein level;
KW   Early protein; Hydrolase; Reference proteome.
FT   CHAIN           1..244
FT                   /note="5'-deoxynucleotidase"
FT                   /id="PRO_0000165218"
FT   CONFLICT        225
FT                   /note="E -> K (in Ref. 3; AAU05298)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   244 AA;  28225 MW;  E6D813D1C78ABE2E CRC64;
     MNQVKTNITR NFPHISRVMI WDLDGTIINS FHRVAPCFDS EGNLDLNKYK NEACKHDLIM
     QDTLLPLVTY MRQCMNDANT LNIICTARLM SKSDYYYLRK QGLRGRGDSN IRVFSRDTLH
     KYFEADKVSE IYHSKDAVYK SYYFGLFKQL YPNADFTMID DHKGVLSAAA SYGFKTLDAQ
     AVNDILSIGV TLIGETFIDE SLEDDNDYQF LADRLQLCWE GMTEEERAEY SCSPQQYIEK
     LKVA